Structural characterization of VGVAPG, an elastin‐derived peptide

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Abstract
Elastic fibers are an important component of the extracellular matrix, providing elasticity and resilience to tissues that require the ability to deform repetitively and reversibly. Among the elastin‐derived peptides, the Val–Gly–Val–Ala–Pro–Gly (VGVAPG) hexapeptide is known for its chemotactic activity and metalloproteinases upregulation properties. As other elastin‐derived peptides, having homologous similar sequences, do not exhibit any biological activity, the following question arises: Does the peptide–receptor interaction need a specific active conformation? Previous experimental studies including NMR and CD spectroscopies did not clearly identify the conformations adopted by the VGVAPG peptide in solution. However, structural predictions made on VGVAPG and related XGXXPG peptides suggested a folded β‐turn conformation. So we undertook a theoretical and experimental study of the VGVAPG peptide. The work presented here, which gives an overall structural description of VGVAPG behavior in water, also provides an additional insight into its structure–activity relationship. Both theoretical and experimental results suggest the existence of an ensemble of rather extended and folded conformations in solution. All the folded structures obtained exhibit a type VIII β‐turn spanning the GVAP sequence. In the lack of any structural information concerning the elastin receptor, these results suggest that such a conformation could be relevant for the peptide–receptor interaction and thus for biological activity. © 2004 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2004
Funding Information
  • ARERS and Comité de l'Aisne de la Ligue contre le Cancer
  • NF is a recipient of a grant from the Ministère de la jeunesse, de l'éducation nationale et de la recherche